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PDBsum entry 3imb

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Top Page protein dna_rna Protein-protein interface(s) links
Hydrolase/DNA PDB id
3imb
Contents
Protein chains
238 a.a.
DNA/RNA
Waters ×729

References listed in PDB file
Key reference
Title How bcni and mvai distinguish w from s
Authors M.Sokolowska, M.Kaus-Drobek, H.Czapinska, G.Tamulaitis, R.H.Szczepanowski, V.Siksnys, M.Bochtler.
Ref. TO BE PUBLISHED ...
Secondary reference #1
Title Monomeric restriction endonuclease bcni in the apo form and in an asymmetric complex with target DNA.
Authors M.Sokolowska, M.Kaus-Drobek, H.Czapinska, G.Tamulaitis, R.H.Szczepanowski, C.Urbanke, V.Siksnys, M.Bochtler.
Ref. J Mol Biol, 2007, 369, 722-734. [DOI no: 10.1016/j.jmb.2007.03.018]
PubMed id 17445830
Full text Abstract
Figure 4.
Figure 4. Apo-BcnI versus BcnI in complex with DNA. (a) A stereo diagram of the superimposed structures. Apo-BcnI is shown in grey, and the BcnI from the cocrystals with DNA is colored as in Figure 3. (b) The C^α trace of apo-BcnI color-ramped according to B-factor. (c) The C^α trace of BcnI from the cocrystals with DNA color-ramped according to B-factor. In the protein region, the correspondence between B-factor and color is identical in (b) and (c). Residues with the lowest B-factors are blue, and residues with the highest B-factors are yellow. DNA is presented in a smoothed representation and colored as in Figure 3.
Figure 6.
Figure 6. Stereo diagram of the BcnI active site in complex with DNA. BcnI active site residues are shown in all-atom representation, metal ions are presented as black and grey spheres, and some key water molecules are shown as red spheres. The 5′-end of the DNA is on the right and the 3′-end is on the left. The 2F[o]–F[c] density was contoured at 1.5 σ and is shown only around the DNA and the nucleophilic water molecule. The assignment of the metal ion that is shown without detailed coordination is very uncertain.
The above figures are reproduced from the cited reference with permission from Elsevier
Secondary reference #2
Title Restriction endonucleases that resemble a component of the bacterial DNA repair machinery.
Authors M.Sokolowska, M.Kaus-Drobek, H.Czapinska, G.Tamulaitis, V.Siksnys, M.Bochtler.
Ref. Cell Mol Life Sci, 2007, 64, 2351-2357.
PubMed id 17568994
Abstract
PROCHECK
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 Headers

 

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